HEADER TRANSCRIPTION 16-NOV-13 4NN2
TITLE PROTEIN CRYSTAL STRUCTURE OF HUMAN BORJESON-FORSSMAN-LEHMANN SYNDROME
TITLE 2 ASSOCIATED PROTEIN PHF6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHD FINGER PROTEIN 6;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 208-333;
COMPND 5 SYNONYM: PHD-LIKE ZINC FINGER PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PHF6, KIAA1823;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1
KEYWDS ZINC FINGER, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LIU,F.LI,J.ZHANG,Y.MEI,J.WU,Y.SHI
REVDAT 3 28-FEB-24 4NN2 1 REMARK SEQADV LINK
REVDAT 2 03-DEC-14 4NN2 1 AUTHOR
REVDAT 1 26-FEB-14 4NN2 0
JRNL AUTH Z.LIU,F.LI,J.ZHANG,Y.MEI,J.WU,Y.SHI
JRNL TITL CRYSTAL STRUCTURE OF THE SECOND EXTENDED PHD DOMAIN OF HUMAN
JRNL TITL 2 PHF6 PROTEIN
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 52630
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2672
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3681
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 264
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.055
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.055
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.877
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1938 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1871 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2583 ; 1.128 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4325 ; 0.730 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 239 ; 6.378 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;28.396 ;23.171
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 372 ;10.209 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;10.572 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 274 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2150 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 457 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 965 ; 0.744 ; 1.215
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 964 ; 0.741 ; 1.214
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1201 ; 1.275 ; 1.814
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4NN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083408.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52631
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.472
REMARK 200 RESOLUTION RANGE LOW (A) : 89.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : 0.50500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMINIUM ACETATE, 0.1M TRI-SODIUM
REMARK 280 CITRATE DEHYDRATE, 30% (W/V) PEG4000, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 541 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 546 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 602 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 579 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 205
REMARK 465 PRO A 206
REMARK 465 SER A 207
REMARK 465 ASN A 332
REMARK 465 ASP A 333
REMARK 465 GLY B 205
REMARK 465 PRO B 206
REMARK 465 SER B 207
REMARK 465 THR B 208
REMARK 465 SER B 256
REMARK 465 ARG B 257
REMARK 465 ALA B 258
REMARK 465 GLU B 259
REMARK 465 GLY B 331
REMARK 465 ASN B 332
REMARK 465 ASP B 333
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 208 OG1 CG2
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 212 SG
REMARK 620 2 CYS A 215 SG 108.6
REMARK 620 3 HIS A 239 ND1 103.8 95.5
REMARK 620 4 CYS A 242 SG 113.2 119.2 114.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 280 SG
REMARK 620 2 CYS A 283 SG 109.8
REMARK 620 3 HIS A 302 ND1 103.5 97.2
REMARK 620 4 CYS A 305 SG 111.0 118.8 114.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 292 SG
REMARK 620 2 CYS A 297 SG 111.8
REMARK 620 3 CYS A 326 SG 117.5 107.7
REMARK 620 4 HIS A 329 ND1 110.1 105.0 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 212 SG
REMARK 620 2 CYS B 215 SG 108.6
REMARK 620 3 HIS B 239 ND1 103.2 94.5
REMARK 620 4 CYS B 242 SG 113.5 118.8 115.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 280 SG
REMARK 620 2 CYS B 283 SG 109.5
REMARK 620 3 HIS B 302 ND1 104.0 98.7
REMARK 620 4 CYS B 305 SG 109.7 119.2 114.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 292 SG
REMARK 620 2 CYS B 297 SG 110.6
REMARK 620 3 CYS B 326 SG 117.1 109.6
REMARK 620 4 HIS B 329 ND1 109.8 107.6 101.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 404
DBREF 4NN2 A 208 333 UNP Q8IWS0 PHF6_HUMAN 208 333
DBREF 4NN2 B 208 333 UNP Q8IWS0 PHF6_HUMAN 208 333
SEQADV 4NN2 GLY A 205 UNP Q8IWS0 EXPRESSION TAG
SEQADV 4NN2 PRO A 206 UNP Q8IWS0 EXPRESSION TAG
SEQADV 4NN2 SER A 207 UNP Q8IWS0 EXPRESSION TAG
SEQADV 4NN2 GLY B 205 UNP Q8IWS0 EXPRESSION TAG
SEQADV 4NN2 PRO B 206 UNP Q8IWS0 EXPRESSION TAG
SEQADV 4NN2 SER B 207 UNP Q8IWS0 EXPRESSION TAG
SEQRES 1 A 129 GLY PRO SER THR ARG PRO LYS CYS GLY PHE CYS HIS VAL
SEQRES 2 A 129 GLY GLU GLU GLU ASN GLU ALA ARG GLY LYS LEU HIS ILE
SEQRES 3 A 129 PHE ASN ALA LYS LYS ALA ALA ALA HIS TYR LYS CYS MET
SEQRES 4 A 129 LEU PHE SER SER GLY THR VAL GLN LEU THR THR THR SER
SEQRES 5 A 129 ARG ALA GLU PHE GLY ASP PHE ASP ILE LYS THR VAL LEU
SEQRES 6 A 129 GLN GLU ILE LYS ARG GLY LYS ARG MET LYS CYS THR LEU
SEQRES 7 A 129 CYS SER GLN PRO GLY ALA THR ILE GLY CYS GLU ILE LYS
SEQRES 8 A 129 ALA CYS VAL LYS THR TYR HIS TYR HIS CYS GLY VAL GLN
SEQRES 9 A 129 ASP LYS ALA LYS TYR ILE GLU ASN MET SER ARG GLY ILE
SEQRES 10 A 129 TYR LYS LEU TYR CYS LYS ASN HIS SER GLY ASN ASP
SEQRES 1 B 129 GLY PRO SER THR ARG PRO LYS CYS GLY PHE CYS HIS VAL
SEQRES 2 B 129 GLY GLU GLU GLU ASN GLU ALA ARG GLY LYS LEU HIS ILE
SEQRES 3 B 129 PHE ASN ALA LYS LYS ALA ALA ALA HIS TYR LYS CYS MET
SEQRES 4 B 129 LEU PHE SER SER GLY THR VAL GLN LEU THR THR THR SER
SEQRES 5 B 129 ARG ALA GLU PHE GLY ASP PHE ASP ILE LYS THR VAL LEU
SEQRES 6 B 129 GLN GLU ILE LYS ARG GLY LYS ARG MET LYS CYS THR LEU
SEQRES 7 B 129 CYS SER GLN PRO GLY ALA THR ILE GLY CYS GLU ILE LYS
SEQRES 8 B 129 ALA CYS VAL LYS THR TYR HIS TYR HIS CYS GLY VAL GLN
SEQRES 9 B 129 ASP LYS ALA LYS TYR ILE GLU ASN MET SER ARG GLY ILE
SEQRES 10 B 129 TYR LYS LEU TYR CYS LYS ASN HIS SER GLY ASN ASP
HET ZN A 401 1
HET ZN A 402 1
HET ZN A 403 1
HET ZN B 401 1
HET ZN B 402 1
HET ZN B 403 1
HET GOL B 404 6
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 6(ZN 2+)
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *264(H2 O)
HELIX 1 1 GLY A 218 GLU A 220 5 3
HELIX 2 2 GLU A 221 GLY A 226 1 6
HELIX 3 3 TYR A 240 PHE A 245 1 6
HELIX 4 4 ASP A 264 LYS A 276 1 13
HELIX 5 5 HIS A 302 ASP A 309 1 8
HELIX 6 6 CYS A 326 SER A 330 5 5
HELIX 7 7 GLY B 218 GLU B 220 5 3
HELIX 8 8 GLU B 221 GLY B 226 1 6
HELIX 9 9 TYR B 240 SER B 246 1 7
HELIX 10 10 ASP B 264 LYS B 276 1 13
HELIX 11 11 HIS B 302 ASP B 309 1 8
HELIX 12 12 MET B 317 GLY B 320 5 4
SHEET 1 A 2 LEU A 228 ILE A 230 0
SHEET 2 A 2 ALA A 237 HIS A 239 -1 O ALA A 238 N HIS A 229
SHEET 1 B 2 ILE A 290 GLY A 291 0
SHEET 2 B 2 THR A 300 TYR A 301 -1 O TYR A 301 N ILE A 290
SHEET 1 C 2 LYS A 312 ASN A 316 0
SHEET 2 C 2 ILE A 321 TYR A 325 -1 O TYR A 325 N LYS A 312
SHEET 1 D 2 LEU B 228 ILE B 230 0
SHEET 2 D 2 ALA B 237 HIS B 239 -1 O ALA B 238 N HIS B 229
SHEET 1 E 2 ILE B 290 GLY B 291 0
SHEET 2 E 2 THR B 300 TYR B 301 -1 O TYR B 301 N ILE B 290
SHEET 1 F 2 LYS B 312 ASN B 316 0
SHEET 2 F 2 ILE B 321 TYR B 325 -1 O TYR B 325 N LYS B 312
LINK SG CYS A 212 ZN ZN A 401 1555 1555 2.41
LINK SG CYS A 215 ZN ZN A 401 1555 1555 2.31
LINK ND1 HIS A 239 ZN ZN A 401 1555 1555 2.17
LINK SG CYS A 242 ZN ZN A 401 1555 1555 2.30
LINK SG CYS A 280 ZN ZN A 402 1555 1555 2.33
LINK SG CYS A 283 ZN ZN A 402 1555 1555 2.35
LINK SG CYS A 292 ZN ZN A 403 1555 1555 2.33
LINK SG CYS A 297 ZN ZN A 403 1555 1555 2.34
LINK ND1 HIS A 302 ZN ZN A 402 1555 1555 2.17
LINK SG CYS A 305 ZN ZN A 402 1555 1555 2.30
LINK SG CYS A 326 ZN ZN A 403 1555 1555 2.33
LINK ND1 HIS A 329 ZN ZN A 403 1555 1555 2.11
LINK SG CYS B 212 ZN ZN B 401 1555 1555 2.36
LINK SG CYS B 215 ZN ZN B 401 1555 1555 2.33
LINK ND1 HIS B 239 ZN ZN B 401 1555 1555 2.15
LINK SG CYS B 242 ZN ZN B 401 1555 1555 2.31
LINK SG CYS B 280 ZN ZN B 402 1555 1555 2.37
LINK SG CYS B 283 ZN ZN B 402 1555 1555 2.32
LINK SG CYS B 292 ZN ZN B 403 1555 1555 2.31
LINK SG CYS B 297 ZN ZN B 403 1555 1555 2.30
LINK ND1 HIS B 302 ZN ZN B 402 1555 1555 2.17
LINK SG CYS B 305 ZN ZN B 402 1555 1555 2.30
LINK SG CYS B 326 ZN ZN B 403 1555 1555 2.31
LINK ND1 HIS B 329 ZN ZN B 403 1555 1555 2.11
SITE 1 AC1 4 CYS A 212 CYS A 215 HIS A 239 CYS A 242
SITE 1 AC2 4 CYS A 280 CYS A 283 HIS A 302 CYS A 305
SITE 1 AC3 4 CYS A 292 CYS A 297 CYS A 326 HIS A 329
SITE 1 AC4 4 CYS B 212 CYS B 215 HIS B 239 CYS B 242
SITE 1 AC5 4 CYS B 280 CYS B 283 HIS B 302 CYS B 305
SITE 1 AC6 4 CYS B 292 CYS B 297 CYS B 326 HIS B 329
SITE 1 AC7 9 HIS A 229 ILE A 230 PHE A 231 ILE A 265
SITE 2 AC7 9 HOH A 511 PHE B 260 GLY B 261 ASP B 262
SITE 3 AC7 9 PHE B 263
CRYST1 102.780 102.780 51.250 90.00 90.00 120.00 P 3 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009730 0.005617 0.000000 0.00000
SCALE2 0.000000 0.011235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019512 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
